1bs8: Difference between revisions

Revision as of 12:58, 21 February 2008

PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER

OverviewOverview

Eubacterial proteins are synthesized with a formyl group at the N-terminus which is hydrolytically removed from the nascent chain by the mononuclear iron enzyme peptide deformylase. Catalytic efficiency strongly depends on the identity of the bound metal. We have determined by X-ray crystallography the Fe2+, Ni2+ and Zn2+ forms of the Escherichia coli enzyme and a structure in complex with the reaction product Met-Ala-Ser. The structure of the complex, with the tripeptide bound at the active site, suggests detailed models for the mechanism of substrate recognition and catalysis. Differences of the protein structures due to the identity of the bound metal are extremely small and account only for the observation that Zn2+ binds more tightly than Fe2+ or Ni2+. The striking loss of catalytic activity of the Zn2+ form could be caused by its reluctance to change between tetrahedral and five-fold metal coordination believed to occur during catalysis. N-terminal formylation and subsequent deformylation

About this StructureAbout this Structure

1BS8 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Full crystallographic information is available from OCA.

ReferenceReference

Iron center, substrate recognition and mechanism of peptide deformylase., Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF, Nat Struct Biol. 1998 Dec;5(12):1053-8. PMID:9846875

Page seeded by OCA on Thu Feb 21 11:58:35 2008

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OCA

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-[[Image:1bs8.gif|left|200px]]<br /><applet load="1bs8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1bs8.gif|left|200px]]<br /><applet load="1bs8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1bs8, resolution 2.20&Aring;" />
 '''PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER'''<br />
 ==Overview==
-Eubacterial proteins are synthesized with a formyl group at the N-terminus, which is hydrolytically removed from the nascent chain by the mononuclear, iron enzyme peptide deformylase. Catalytic efficiency strongly depends on, the identity of the bound metal. We have determined by X-ray, crystallography the Fe2+, Ni2+ and Zn2+ forms of the Escherichia coli, enzyme and a structure in complex with the reaction product Met-Ala-Ser., The structure of the complex, with the tripeptide bound at the active, site, suggests detailed models for the mechanism of substrate recognition, and catalysis. Differences of the protein structures due to the identity, of the bound metal are extremely small and account only for the, observation that Zn2+ binds more tightly than Fe2+ or Ni2+. The striking, loss of catalytic activity of the Zn2+ form could be caused by its, reluctance to change between tetrahedral and five-fold metal coordination, believed to occur during catalysis. N-terminal formylation and subsequent, deformylation
+Eubacterial proteins are synthesized with a formyl group at the N-terminus which is hydrolytically removed from the nascent chain by the mononuclear iron enzyme peptide deformylase. Catalytic efficiency strongly depends on the identity of the bound metal. We have determined by X-ray crystallography the Fe2+, Ni2+ and Zn2+ forms of the Escherichia coli enzyme and a structure in complex with the reaction product Met-Ala-Ser. The structure of the complex, with the tripeptide bound at the active site, suggests detailed models for the mechanism of substrate recognition and catalysis. Differences of the protein structures due to the identity of the bound metal are extremely small and account only for the observation that Zn2+ binds more tightly than Fe2+ or Ni2+. The striking loss of catalytic activity of the Zn2+ form could be caused by its reluctance to change between tetrahedral and five-fold metal coordination believed to occur during catalysis. N-terminal formylation and subsequent deformylation
 ==About this Structure==
-BS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BS8 OCA].
+BS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BS8 OCA].
 ==Reference==
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 [[Category: Schlichting, I.]]
 [[Category: Schultz, S.]]
-[[Category: Wagner, A.F.V.]]
+[[Category: Wagner, A F.V.]]
 [[Category: SO4]]
 [[Category: ZN]]
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 [[Category: iron metalloprotease; protein synthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:52:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:35 2008''